Evidence map›Paper›PMID 24375403›Full record

ArticleThe Journal of biological chemistry2014

Rod visual pigment optimizes active state to achieve efficient G protein activation as compared with cone visual pigments.

Keiichi Kojima, Yasushi Imamoto, Ryo Maeda, Takahiro Yamashita, Yoshinori Shichida

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.6field-weighted citation impact, top 38% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Structure of human green cone opsin yields insights into mechanisms underlying the rapid decay of its active, signaling state.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Glu102Biochemistry · 2024
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Stereospecific modulation of dimeric rhodopsin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Evolutionary steps involving counterion displacement in a tunicate opsin.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Adaptation of cone pigments found in green rods for scotopic vision through a single amino acid mutation.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Photocyclic behavior of rhodopsin induced by an atypical isomerization mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Article
  18. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Keiichi KojimaFrom the Department of Biophysics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.
Yasushi Imamoto
Ryo Maeda
Takahiro Yamashita
Yoshinori Shichida
Kyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Most vertebrate retinas contain two types of photoreceptor cells, rods and cones, which show different photoresponses to mediate scotopic and photopic vision, respectively. These cells contain different types of visual pigments, rhodopsin and cone visual pigments, respectively, but little is known about the molecular properties of cone visual pigments under physiological conditions, making it difficult to link the molecular properties of rhodopsin and cone visual pigments with the differences in photoresponse between rods and cones. Here we prepared bovine and mouse rhodopsin (bvRh and mRh) and chicken and mouse green-sensitive cone visual pigments (cG and mG) embedded in nanodiscs and applied time-resolved fluorescence spectroscopy to compare their Gt activation efficiencies. Rhodopsin exhibited greater Gt activation efficiencies than cone visual pigments. Especially, the Gt activation efficiency of mRh was about 2.5-fold greater than that of mG at 37 °C, which is consistent with our previous electrophysiological data of knock-in mice. Although the active state (Meta-II) was in equilibrium with inactive states (Meta-I and Meta-III), quantitative determination of Meta-II in the equilibrium showed that the Gt activation efficiency per Meta-II of bvRh was also greater than those of cG and mG. These results indicated that efficient Gt activation by rhodopsin, resulting from an optimized active state of rhodopsin, is one of the causes of the high amplification efficiency of rods.

Indexed as

AnimalsCattleChickensHEK293 CellsHumansKineticsLightMiceRetinal Cone Photoreceptor CellsRetinal PigmentsRetinal Rod Photoreceptor CellsRhodopsinRod Cell Outer SegmentSpectrum AnalysisTransducinRetinal PigmentsRhodopsinTransducinFluorescence SpectroscopyG Protein Activation EfficiencyG Protein-coupled Receptors (GPCR)Membrane BilayerMembrane ProteinsRhodopsinUV Spectroscopy

Identifiers

PMID24375403
PMCPMC3931065
OpenAlexW2046686103

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.